1bbw

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(New page: 200px<br /><applet load="1bbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bbw, resolution 2.7&Aring;" /> '''LYSYL-TRNA SYNTHETASE...)
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'''LYSYL-TRNA SYNTHETASE (LYSS)'''<br />
'''LYSYL-TRNA SYNTHETASE (LYSS)'''<br />
==Overview==
==Overview==
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Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA, synthetases and catalyses the specific aminoacylation of tRNA(Lys). The, crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from, Escherichia coli has been determined to 2.7 A resolution in the unliganded, form and in a complex with the lysine substrate. A comparison between the, unliganded and lysine-bound structures reveals major conformational, changes upon lysine binding. The lysine substrate is involved in a network, of hydrogen bonds. Two of these interactions, one between the alpha-amino, group and the carbonyl oxygen of Gly 216 and the other between the, carboxylate group and the side chain of Arg 262, trigger a subtle and, complicated reorganization of the active site, involving the ordering of, two loops (residues 215-217 and 444-455), a change in conformation of, residues 393-409, and a rotation of a 4-helix bundle domain (located, between motif 2 and 3) by 10 degrees. The result of these changes is a, closing up of the active site upon lysine binding.
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Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.
==About this Structure==
==About this Structure==
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1BBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BBW OCA].
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1BBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBW OCA].
==Reference==
==Reference==
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[[Category: protein biosynthesis]]
[[Category: protein biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:31:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:37 2008''

Revision as of 09:53, 21 February 2008


1bbw, resolution 2.7Å

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LYSYL-TRNA SYNTHETASE (LYSS)

Overview

Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.

About this Structure

1BBW is a Single protein structure of sequence from Escherichia coli. Active as Lysine--tRNA ligase, with EC number 6.1.1.6 Full crystallographic information is available from OCA.

Reference

Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding., Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P, Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850

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